Anti-β-Dystroglycan (Tyr-892), Phosphospecific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q14118 |
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Reactivity | Bovine |
Host | Mouse |
Clonality | Mouse Monoclonal |
Isotype | IgG1 |
Clone Names | M117 |
Calculated MW | 97441 Da |
Gene ID | 1605 |
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Target/Specificity | Dystroglycans are essential elements of the neuromuscular junction (NMJ). The gene for dystroglycan is expressed as a precursor protein that is post-translationally cleaved into a 156 kDa extracellular peripheral membrane protein called α-dystroglycan and a 43 kDa transmembrane protein, β-Dystroglycan. The latter protein contains a PPxY motif that promotes binding to WW domain-containing proteins, such as utrophin and dystrophin. Phosphorylation at tyrosine 892 within the PPxY motif may regulate c-Src interactions with β-Dystroglycan, as well as inhibit interactions with WW domain proteins. In skeletal muscle, β-Dystroglycan is normally localized to the plasma membrane, however phosphorylation of Tyr-892 leads to localization of β-Dystroglycan to endosomal compartments along with c-Src. Thus, phosphorylation at Tyr-892 may have important roles in altering the localization of β-Dystroglycan during NMJ formation. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Anti-β-Dystroglycan (Tyr-892), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |
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Background
Dystroglycans are essential elements of the neuromuscular junction (NMJ). The gene for dystroglycan is expressed as a precursor protein that is post-translationally cleaved into a 156 kDa extracellular peripheral membrane protein called α-dystroglycan and a 43 kDa transmembrane protein, β-Dystroglycan. The latter protein contains a PPxY motif that promotes binding to WW domain-containing proteins, such as utrophin and dystrophin. Phosphorylation at tyrosine 892 within the PPxY motif may regulate c-Src interactions with β-Dystroglycan, as well as inhibit interactions with WW domain proteins. In skeletal muscle, β-Dystroglycan is normally localized to the plasma membrane, however phosphorylation of Tyr-892 leads to localization of β-Dystroglycan to endosomal compartments along with c-Src. Thus, phosphorylation at Tyr-892 may have important roles in altering the localization of β-Dystroglycan during NMJ formation.
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